Qualification of biophysical methods for the analysis of protein therapeutics

Biophysics for Therapeutic Protein Development

Volumn , Issue , 2013, Pages 99-126

  Jiang, Yijia ^a   Li, Cynthia ^a   Gabrielson, John ^a  

^a AMGEN INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84877919996     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-4316-2_5     Document Type: Chapter

References (111)

1. Affolter S, Ritter A, Schmid M (2001) Interlaboratory tests on polymers by differential scanning calorimetry (DSC): determination of glass transition temperature (Tg). Macromol Mater Eng 286(10):605-610.
2. Alexander DM, Veltman AM (1988) Particulate contamination in solutions of antibiotics packed as dry powders in vials. J Pharm Pharmacol 40(5):358-359.
3. Arthur KK et al (2009) Detection of protein aggregates by sedimentation velocity analytical ultracentrifugation (SV-AUC): sources of variability and their relative importance. J Pharm Sci 98(10):3522-3539.
4. Berkowitz SA (2006) Role of analytical ultracentrifugation in assessing the aggregation of protein biopharmaceuticals. AAPS J 8(3):590-605.
5. Bruylants G, Wouters J, Michaux C (2005) Differential scanning calorimetry in life science: thermodynamics, stability, molecular recognition and application in drug design. Curr Med Chem 12(17):2011-2020.
6. Byler DM, Susi H (1986) Examination of the secondary structure of proteins by deconvoluted FTIR spectra. Biopolymers 25:469-487.
7. Cao S, Jiao N, Jiang Y, Mire-Sluis A, Narhi LO (2009) Sub-visible particle quantitation in protein therapeutics. Pharmeuropa Bio & Scientific Notes 73-79.
8. Cao S, Jiang Y, Narhi LO (2010) A light obscuration method specific for quantifying subvisible particles in protein therapeutics. US Pharmacoepial Forum 36(3):824-834.
9. Cao S, Narhi LO, Jiang Y, Rajan RS (2012) Analytical methods to measure sub-visible particulates. In: Mahler HC, Jiskoot W (eds) Analysis of aggregates and particles in protein pharmaceuticals. Wiley, New York.
10. Carpenter JF, Prestrelski SJ, Dong A (1998) Application of infrared spectroscopy to development of stable lyophilized protein formulations. Eur J Pharm Biopharm 45(3):231-238.
11. Carpenter JF et al (2009) Overlooking subvisible particles in therapeutic protein products: gaps that may compromise product quality. J Pharm Sci 98(4):1201-1205.
12. Carpenter JF et al (2010) Potential inaccurate quantitation and sizing of protein aggregates by size exclusion chromatography: essential need to use orthogonal methods to assure the quality of therapeutic protein products. J Pharm Sci 99(5):2200-2208.
13. Celej MS, Dassie SA, González M, Bianconi ML, Fidelio GD (2006) Differential scanning calorimetry as a tool to estimate binding parameters in multiligand binding proteins. Anal Biochem 350(2):277-284.
14. Chan CC, Lam H, Zhang XM (2011) Practical approaches to method validation and essential instrument qualification. Wiley, New York.
15. Chiu MH, Prenner EJ (2011) Differential scanning calorimetry: an invaluable tool for a detailed thermodynamic characterization of macromolecules and their interactions. J Pharm Bioallied Sci 3(1):39-59.
16. Coligan JE et al (2001) Measuring protein thermostability by differential scanning calorimetry. In: Makhatadze GI (ed) Current protocols in protein science/editorial board. Wiley, New York.
17. Council of Europe (2007) Particulate contamination: sub-visible particles, general chapter 2.9.19.
18. Council of Europe, Strasbourg Cover TM, Hart PE (1967) Nearest neighbor pattern classification. IEEE Trans Inf Theory IT-13(1):21-27.
19. D'antonio J, Murphy BM, Manning MC, Al-Azzam WA (2012) Comparability of protein therapeutics:quantitative comparison of second-derivative amide I infrared spectra. J Pharm Sci. doi:10.1002/jps.23133.
20. Dam J et al (2004) Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity concentration profiles. In: Methods in enzymology. Academic. pp 185-212.
21. Drechsler A, Miles AJ, Norton RC, Wallace BA, Separovic F (2009) Effect of lipid on the conformation of the n-terminal region of equinatoxin II: a synchrotron radiation CD study. Eur Biophys J 39:121-127.
22. Driscoll DF (2004) Examination of selection of light-scattering and light-obscuration acceptance criteria for lipid injectable emulsions. Pharm Forum 30:2244-2253.
23. Fu K, Griebenow K, Hsieh L, Klibanov AM, Langer R (1999) FTIR characterization of the secondary structure of proteins encapsulated within PLGA microspheres. J Controlled Release 58:357-366.
24. Gabrielson JP, Arthur KK (2011) Measuring low levels of protein aggregation by sedimentation velocity. Methods 54(1):83-91.
25. Gabrielson JP et al (2007a) Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation, and sedimentation velocity. J Pharm Sci 96(2):268-279.
26. Gabrielson JP et al (2007b) Sedimentation velocity analytical ultracentrifugation and SEDFIT/ c(s): limits of quantitation for a monoclonal antibody system. Anal Biochem 361:24-30.
27. Gabrielson JP, Arthur KK, Stoner MR et al (2010) Precision of protein aggregation measurements by sedimentation velocity analytical ultracentrifugation in biopharmaceutical applications. Anal Biochem 396(2):231-241.
28. Gmelin E, Sarge St.M (1995) Calibration of differential scanning calorimeters. IUPAC, Pure Appl Chem 67:1789-1800.
29. Greenfield NJ (1996) Methods to estimate conformation of proteins and polypeptides from CD data. Anal Biochem 235(1):1-10.
30. Greenfield NJ, Fasman GD (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8:4108-4116.
31. Gross PC, Zeppezauer M (2010) Infrared spectroscopy for biopharmaceutical protein analysis. J Pharm Biomed Anal 53:29-36.
32. Haines-Nutt RF, Munton TJ (1984) Particle size measurement in intravenous fluids. J Pharm Pharmacol 36(8):534-536.
33. Haris PI, Chapman D (1995) The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolym (Pept Sci) 37:251-263.
34. Huang CT, Sharma D, Oma P, Krishnamurthy R (2009) Quantitation of protein particles in parenteral solutions using micro-flow imaging. J Pharm Sci 98(9):3058-3071.
35. ICH M4Q (2001) The common technical document for the registration of pharmaceuticals for human use: quality. US Department of Health and Services, FDA, CDER.
36. ICH Q2(R1) (2005) Validation of analytical procedures: test and methodology. In: ICH Harmonised Tripartite guideline in international conference on harmonisation of technical requirements for registration of pharmaceuticals for human use.
37. ICH Q5E (2005) Comparability of biotechnological/biological products subject to changes in their manufacturing process. US Department of Health and Services, FDA, CDER & CBER.
38. ICH Q6B (1999) Test procedures and acceptance criteria for biotechnological and biological products.
39. Jiang Y, Narhi LO (2006) Applying selective biophysical techniques in assessing the comparability of protein therapeutics - case studies. J Am Pharm Rev 9(5):34-43.
40. Jiang Y, Li C, Ramachander R, Wen J, Narhi LO (2008) Meeting new regulatory expectations of characterization methods-Qualification of biophysical analyses. J Am Pharm Rev February, online issue, Russell Publishing. http://pharmoutsourcing.com/ViewArticle.aspx?ContentID=2221. Accessed 7 Feb 2012.
41. Jiang Y, Li C, Nguyen X, Muzammil S, Towers E, Gabrielson JP, Narhi LO (2011) Qualification of FTIR spectroscopic method for protein secondary structural analysis. J Pharm Sci 100(11):4631-4641.
42. Johnson WC Jr (1988) Secondary structure of proteins through circular dichroism spectroscopy. Annu Rev Biophys Biophys Chem 17:145-166.
43. Johnson WC Jr (1999a) Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins 35(3):307-312.
44. Johnson WC (1999b) Analysing protein circular dichroism spectra for accurate secondary structures. Proteins 35(3):307-312.
45. Johnson CR, Morin PE, Arrowsmith CH, Freire E (1995) Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of p53 tumor suppressor. Biochemistry 34(16):5309-5316.
46. Johnston MJW, Frahm G, Li X, Durocher Y, Hefford MA (2011) O-linked glycosylation leads to decreased thermal stability of interferon alpha 2b as measured by two orthogonal techniques. Pharm Res 28(7):1661-1667.
47. Jones C et al (2004) Val-CiD Best Practice Guide: CD spectroscopy for the quality control of biopharmaceuticals. National Physical Laboratory. DQL-AS 008 ISSN: 1744-0602. British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire, LS23 7BQ Kelly SM,.
48. Kelly S.M. Jess TJ, Price NC (2005) How to study proteins by circular dichroism. Biochim Biophys Acta 1751:119-139.
49. Kendrick BS, Dong A, Allison SD, Manning MC, Carpenter JF (1996) Quantitation of overlap of infrared second derivative spectra to determine structural similarity between proteins. J Pharm Sci 85:155-158.
50. Kendrick BS et al (2001) Online size-exclusion high-performance liquid chromatography light scattering and differential refractometry methods to determine degree of polymer conjugation to proteins and protein-protein or protein-ligand association states. Anal Biochem 299(2):136-146.
51. King SM, Johnson WC (1999) Assigning secondary structure from protein coordinate data. Proteins 35:313-320.
52. Kong J, Yu S (2007) Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim Biophys Sin 39(8):549-559.
53. Laue TM et al (1992) Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding SE, Rowe AJ, Horton JC (eds) Analytical ultracentrifugation in biochemistry and polymer science. Royal Society of Chemistry, Cambridge, pp 90-125.
54. Lebowitz J, Lewis MS, Schuck P (2002) Modern analytical ultracentrifugation in protein science:a tutorial review. Protein Sci 11(9):2067-2079.
55. Lees JG, Wallace BA (2002) Synchrotron radiation circular dichroism and conventional circular dichroism spectroscopy: a Comparison. Spectroscopy 16:121-125.
56. Lees JG, Miles AJ, Wien F, Wallace BA (2006) A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22:1955-1962.
57. Li C, Nguyen X, Narhi LO, Chemmalil L, Towers E, Muzammil S, Gabrielson JP, Jiang Y (2011) Applications of circular dichroism for structural analysis of proteins: qualification of near- and far-UV CD for protein higher order structural analysis. J Pharm Sci 100(11):4642-4654.
58. Lopez MO, Freire E (1987) Dynamic analysis of differential scanning calorimetry data. Biophys Chem 27(1):87-96.
59. Mahler HC, Friess W, Grauschopf U, Kies S (2009) Protein aggregation: pathways, induction factors and analysis. J Pharm Sci 98:2909-2934.
60. Manning MC, Woody RW (1989) Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor. Biochemistry 28:8609-8613.
61. Meersman F, Atilgan C, Miles AJ, Bader R, Shang W, Matagne A, Wallace BA, Koch MHJ (2010) Consistent picture of the reversible thermal unfolding of hen egg-white lysozyme from experiment and molecular dynamics. Biophysical J 99:2255-2263.
62. Miles AJ, Wallace BA (2006) Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics. Chem Soc Reviews 35:39-51.
63. Miles AJ, Wien F, Lees JG, Rodger A, Janes RW, Wallace BA (2003) Calibration and standardisation of synchrotron radiation circular dichroism (SRCD) amplitudes and conventional circular dichroism (CD) spectrophotometers. Spectroscopy 17:653-661.
64. Miles AJ, Wien F, Wallace BA (2004) Redetermination of the extinction coefficient of camphor-bsulfonic acid, A calibration standard for circular dichroism spectroscopy. Anal Biochem 335:338-339.
65. Miles AJ, Wien F, Lees JG, Wallace BA (2005) Calibration and standardisation of synchrotron radiation and conventional circular dichroism spectrometers. Part 2: factors affecting magnitude and wavelength. Spectroscopy 19:43-51.
66. Miles AJ, Hoffman SV, Tao Y, Janes RW, Wallace BA (2007) Synchrotron radiation circular dichroism (SRCD) spectroscopy: new beamlines and new applications in biology. Spectroscopy 21:245-255.
67. Narhi LO, Jiang Y, Cao S, Benedek K, Shnek D (2009) A critical review of analytical methods for subvisible and visible particles. Curr Pharm Biotechnol 10(4):373-381.
68. Pekar A, Sukumar M (2007) Quantitation of aggregates in therapeutic proteins using sedimentation velocity analytical ultracentrifugation: practical considerations that affect precision and accuracy. Anal Biochem 367:225-237.
69. Perczel A, Fasman GD (1993) Effect of spectral window size on circular dichroism spectra deconvolution of proteins. Biophys Chem 48:19-29.
70. Perczel A, Hollosi M, Tusnady G, Fasman GD (1991) Convex constraint analysis: a natural deconvolution of circular dichroism curves of proteins. Protein Eng 4:669-679.
71. Philo JS (2006) Is any measurement method optimal for all aggregate sizes and types? AAPS J 8(3):564-571.
72. Powl AM, O'Reilly AO, Miles AM, Wallace BA (2010) Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly. Proc Natl Acad Sci 107:14064-14069.
73. Prestrelski S, Tedeschi N, Arakawa T, Carpenter J (1993) Biophys J 65(2):661-671.
74. Protasevich I, Yang Z, Wang C, Atwell S, Zhao X, Emtage S, Wetmore D, Hunt JF, Brouillette CG (2010) Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. Protein Sci 19(10):1917-1931.
75. Pyrpassopoulos S, Vlassi M, Tsortos A, Papanikolau Y, Petratos K, Vorgias CE, Nounesis G (2006) Equilibrium heat-induced denaturation of chitinase 40 from Streptomyces thermoviolaceus. Proteins 64(2):513-523.
76. Ravi J, Rakowska PD, Garfagnini T et al (2010) International comparability in spectroscopic measurements of protein structure by circular dichroism: CCQM-P59.1, Metrologia 47(6):631-641.
77. Ravi J, Schiffmann D, Tantra R et al (2010) International comparability in spectroscopic measurements of protein structure by circular dichroism: CCQM P59, Metrologia 47:1A.
78. Schiffmann D, Butterfield DM, Yardley RE, Knight A, Windsor SA, Jones C (2004) Val-CiD Appendix A: CD spectroscopy: an inter-laboratory study. DQL-AS 009 ISSN: 1744-0602.
79. Schmid M (2012) Precision of DSC measurements: results of interlaboratory tests. http://www. eurostar-science.org/MAP1/Schmid.pdf. Accessed 7 Feb 2012.
80. Schuck P et al (2002) Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys J 82(2):1096-1111.
81. Sharma DK, King D, Oma P, Merchant C (2010a) Micro-flow imaging: flow microscopy applied to sub-visible particulate analysis in protein formulations. AAPS J 12(3):455-464.
82. Sharma DK, Peter O, Pollo MJ, Sukumar M (2010b) Quantification and characterization of subvisible proteinaceous particles in opalescent mab formulations using micro-flow imaging. J Pharm Sci 99(6):2628-2642.
83. Sharma DK, King D, Merchant C (2011) Reference material development for calibration and verification of image-based particle analyzers. Int J Pharm 416(1):293-295.
84. Shire SJ (1994) Analytical ultracentrifugation and its use in biotechnology. In: Schuster TM, Laue TM (eds) Modern analytical ultracentrifugation. Birkhauser, Boston.
85. Surewicz WK, Mantsch HH (1988) New insight into protein conformation from infrared spectroscopy. Biochim Biophys Acta 952:115-130.
86. Susi H, Byler M (1986) Resolution enhanced fourier transform infrared spectroscopy of enzymes. Meth Enzymol 130:290-311.
87. Susi H, Byler M (1987) Fourier transform infrared study of proteins with parallel b-chains. Arch Biochem Biophys 258(2):465-469.
88. Taylor JR (1997) An introduction to error analysis: the study of uncertainties in physical measurements, 2nd edn. University Science Books, Sausalito.
89. Taylor SA, Spence J (1983) Particles in small volume injections. J Pharm Pharmacol 35(12):769-773.
90. TQ Analyst Algorithm (2007-2010) Thermo OMNIC software manual, Thermo Electron Scientific Instruments, LLC., Madison, WI, USA (part of Thermo Fisher Scientific Inc.).
91. United States Pharmacopeial Convention, Inc (2009) Particular matter in injections, general chapter <788>, USP 32, NF 27. United States Pharmacopeial Convention, Inc., Rockville.
92. Van Stokkum IHM, Spoelder HJW, Bloemendal M, Van Grondelle R, Groen FCA (1990) Estimation of protein secondary structure and error analysis from CD spectra. Anal Biochem 191:110-118.
93. Vedantham G, Sparks G, Sane SU, Tzannis S, Przybycien TM (2000) A holistic approach for protein secondary structure estimation from infrared spectra in H2O solutions. Anal Biochem 285:33-49.
94. Venyaminov SW, Baikalov I, Chuen-Shang C, Yang JT (1991) Some problems of CD analysis of protein conformation. Anal Biochem 198:250-255.
95. Vonhoffa S, Condliffeb J, Schiffterb H (2010) Implementation of an FTIR calibration curve for fast and objective determination of changes in protein secondary structure during formulation development. J Pharm Biomed Anal 51(1):39-45.
96. Wallace BA (2005) Shining new light on protein structure and function thru synchrotron radiation circular dichroism (SRCD) spectroscopy. Australian Biochemist 36:47-50.
97. Wallace BA, Janes RW (2010) Synchrotron radiation circular dichroism (SRCD) spectroscopy: an enhanced method for examining protein conformations and protein interactions. Biochem Soc Trans 38:861-873.
98. Wallace BA, Whitmore L, Janes RW (2006) The protein circular dichroism data bank (PCDDB):a bioinformatics and spectroscopic resource. Proteins 62:1-3.
99. Weissburg RP, Burris FE, Ferrell TK, Montgomery ER (2002) Validation of DSC and TGA for pharmaceutical analysis under current good Manufacturing Practices (cGMP). Am Pharm Rev 5(2):76-81.
100. Wen J, Arakawa T, Philo JS (1996) Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal Biochem 240(2):155-166.
101. Wen J, Jiang Y, Narhi LO (2008) Effect of carbohydrate on thermal stability of antibodies. Am Pharm Rev 11:98-104.
102. Wen J, Arthur K, Chemmalil L, Muzammil S, Gabrielson JP, Jiang Y (2011) Applications of differential scanning calorimetry for thermal stability analysis of proteins: qualification of DSC. J Pharm Sci. doi:10.1002/jps.22820.
103. Whitmore L, Wallace BA (2004) DICHROWEB, An online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32:668-673.
104. Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89:392-400.
105. Woody RW (1994) Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur Biophys J 23:253-262.
106. Woody RW (1996) Theory of circular dichroism of proteins, circular dichroism and the conformational analysis of biomolecules. In: Fasman GD (ed) Circular dichroism and the conformational analysis of biomolecules. Plenum, New York.
107. Wuchner K, Büchler J, Spycher R, Dalmonte P, Volkin DB (2010) Development of a microflow digital imaging assay to characterize protein particulates during storage of a high concentration IgG1 monoclonal antibody formulation. J Pharm Sci 99(8):3343-3361.
108. Wyatt PJ (1993) Light scattering and the absolute characterization of macromolecules. Anal Chim Acta 272:1-40.
109. Yang JT, Wu CSC, Martinez HM (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol 130:208-269.
110. Yoshii K (1997) Application of differential scanning calorimetry to the estimation of drug purity:various problems and their solutions in purity analysis. Chem Pharm Bull 45(2):338-343.
111. Zölls S, Tantipolphan R, Wiggenhorn M, Winter G, Jiskoot W, Friess W, Hawe A (2011) Particles in therapeutic protein formulations, Part 1: overview of analytical methods. J Pharm Sci. doi:10.1002/jps.23001.